FCGR2_MOUSE
ID FCGR2_MOUSE Reviewed; 330 AA.
AC P08101; P08102; P12316; P97917; Q60938; Q60939; Q60940; Q61170; Q61558;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor II;
DE AltName: Full=Fc gamma receptor IIB;
DE Short=Fc-gamma RII;
DE Short=Fc-gamma-RIIB;
DE Short=FcRII;
DE AltName: Full=IgG Fc receptor II beta;
DE AltName: Full=Lymphocyte antigen 17;
DE Short=Ly-17;
DE AltName: CD_antigen=CD32;
DE Flags: Precursor;
GN Name=Fcgr2; Synonyms=Fcgr2b, Ly-17;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-51 (ISOFORMS IIB1
RP AND IIB2).
RX PubMed=2946078; DOI=10.1126/science.2946078;
RA Ravetch J.V., Luster A.D., Weinshank R., Kochan J., Pavlovec A.,
RA Portnoy D.A., Hulmes J., Pan Y.-C.E., Unkeless J.C.;
RT "Structural heterogeneity and functional domains of murine immunoglobulin G
RT Fc receptors.";
RL Science 234:718-725(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
RC TISSUE=Macrophage;
RX PubMed=3024012; DOI=10.1038/324372a0;
RA Lewis V.A., Koch T., Plutner H., Mellman I.;
RT "A complementary DNA clone for a macrophage-lymphocyte Fc receptor.";
RL Nature 324:372-375(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM IIB1).
RX PubMed=2957319; DOI=10.1007/bf00365906;
RA Hogarth P.M., Hibbs M.L., Bonadonna L., Scott B.M., Witort E.,
RA Pietersz G.A., McKenzie I.F.C.;
RT "The mouse Fc receptor for IgG (Ly-17): molecular cloning and
RT specificity.";
RL Immunogenetics 26:161-168(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM IIB1), POLYMORPHISM, AND
RP VARIANTS.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=2138587; DOI=10.1007/bf00211557;
RA Lah M., Quelch K., Deacon N.J., McKenzie I.F., Hogarth P.M.;
RT "Identification of the mouse beta Fc gamma RII polymorphism by direct
RT sequencing of amplified genomic DNA.";
RL Immunogenetics 31:202-206(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORMS IIB1 AND IIB2).
RX PubMed=1824594;
RA Hogarth P.M., Witort E., Hulett M.D., Bonnerot C., Even J., Fridman W.H.,
RA McKenzie I.F.C.;
RT "Structure of the mouse beta Fc gamma receptor II gene.";
RL J. Immunol. 146:369-376(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB1').
RC STRAIN=DBA/2J; TISSUE=Mast cell;
RX PubMed=8683114;
RA Latour S., Fridman W.H., Daeron M.;
RT "Identification, molecular cloning, biologic properties, and tissue
RT distribution of a novel isoform of murine low-affinity IgG receptor
RT homologous to human Fc gamma RIIB1.";
RL J. Immunol. 157:189-197(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-330 (ISOFORMS IIB1 AND IIB2).
RC STRAIN=DBA/2J, and NZB; TISSUE=Spleen;
RX PubMed=8537115; DOI=10.1007/bf00186618;
RA Sawchuk D.J., Mahmoudi M., Cairns E., Sinclair N.R.S.;
RT "Nonsynonymous mutations in an Fc-receptor structural gene in NZB mice.";
RL Immunogenetics 43:112-113(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-45.
RX PubMed=2944118; DOI=10.1073/pnas.83.18.6980;
RA Hibbs M.L., Walker I.D., Kirszbaum L., Peitersz G.A., Deacon N.J.,
RA Chambers G.W., McKenzie I.F.C., Hogarth P.M.;
RT "The murine Fc receptor for immunoglobulin: purification, partial amino
RT acid sequence, and isolation of cDNA clones.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6980-6984(1986).
RN [9]
RP CHARACTERIZATION OF ISOFORM IIB3.
RC TISSUE=Macrophage;
RX PubMed=8398981; DOI=10.1093/intimm/5.8.859;
RA Tartour E., de la Salle H., de la Salle C., Teillaud C., Camoin L.,
RA Galinha A., Latour S., Hanau D., Fridman W.H., Sautes C.;
RT "Identification, in mouse macrophages and in serum, of a soluble receptor
RT for the Fc portion of IgG (Fc gamma R) encoded by an alternatively spliced
RT transcript of the Fc gamma RII gene.";
RL Int. Immunol. 5:859-868(1993).
RN [10]
RP PHOSPHORYLATION, AND INTERACTION WITH LYN.
RX PubMed=9469421;
RA Malbec O., Fong D.C., Turner M., Tybulewicz V.L., Cambier J.C.,
RA Fridman W.H., Daeron M.;
RT "Fc epsilon receptor I-associated lyn-dependent phosphorylation of Fc gamma
RT receptor IIB during negative regulation of mast cell activation.";
RL J. Immunol. 160:1647-1658(1998).
RN [11]
RP PHOSPHORYLATION AT TYR-290; TYR-309 AND TYR-326.
RX PubMed=11035084; DOI=10.4049/jimmunol.165.8.4453;
RA Fong D.C., Brauweiler A., Minskoff S.A., Bruhns P., Tamir I., Mellman I.,
RA Daeron M., Cambier J.C.;
RT "Mutational analysis reveals multiple distinct sites within Fc gamma
RT receptor IIB that function in inhibitory signaling.";
RL J. Immunol. 165:4453-4462(2000).
CC -!- FUNCTION: Receptor for the Fc region of complexed immunoglobulins
CC gamma. Low affinity receptor. Involved in a variety of effector and
CC regulatory functions such as phagocytosis of antigen-antibody complexes
CC from the circulation and modulation of antibody production by B-cells.
CC Isoform IIB1 and isoform IIB1' form caps but fail to mediate
CC endocytosis or phagocytosis. Isoform IIB2 can mediate the endocytosis
CC of soluble immune complexes via clathrin-coated pits. Isoform IIB1 and
CC isoform IIB2 can down-regulate B-cell, T-cell, and mast cell activation
CC when coaggregated to B-cell receptors for AG (BCR), T-cell receptors
CC for AG (TCR), and Fc receptors, respectively.
CC -!- SUBUNIT: Interacts with FGR (By similarity). Interacts with LYN.
CC {ECO:0000250, ECO:0000269|PubMed:9469421}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform IIB1]: Cytoplasm, cytoskeleton.
CC Note=Binds the cytoskeleton and is not localized in endocytotic pits.
CC -!- SUBCELLULAR LOCATION: [Isoform IIB3]: Secreted. Note=Released as a
CC soluble molecule.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=IIB1; Synonyms=Beta-1;
CC IsoId=P08101-1; Sequence=Displayed;
CC Name=IIB2; Synonyms=Beta-2;
CC IsoId=P08101-2; Sequence=VSP_002640;
CC Name=IIB1'; Synonyms=Beta-1';
CC IsoId=P08101-3; Sequence=VSP_002641;
CC Name=IIB3; Synonyms=Beta-3;
CC IsoId=P08101-4; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Widely expressed by cells of hemopoietic origin.
CC The isoforms are differentially expressed. Isoform IIB1 is
CC preferentially expressed by cells of the lymphoid lineage, isoform IIB2
CC by cells of the myeloid lineage, and isoform IIB3 is released by
CC macrophages and is present in the serum. Isoform IIB1' is expressed in
CC myeloid and lymphoid cell lines, in normal spleen cells, and in resting
CC or LPS-activated B-cells but is not detected in mesenteric lymph node
CC cells.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC Another tyrosine-containing sequence, more C-terminal, accounts for the
CC ability of isoform IIB2 to trigger the phagocytosis of particulate
CC immuno complexes.
CC -!- PTM: Glycosylated.
CC -!- PTM: When coaggregated to BCR, isoform IIB1 and isoform IIB1' become
CC tyrosine phosphorylated and bind to the SH2 domains of the protein
CC tyrosine phosphatase PTPC1. Phosphorylated by SRC-type Tyr-kinases such
CC as LYN, BLK, FYN and SYK (By similarity). {ECO:0000250}.
CC -!- POLYMORPHISM: Ly-17 alloantigenic system involves residues 116 and 161.
CC Ly-17.1 mice are Pro-116 and Glu-161; Ly-17.2 mice are Leu-116 and Leu-
CC 161. These polymorphisms do not affect IgG binding.
CC {ECO:0000269|PubMed:2138587}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28309.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M16367; AAA37608.1; -; mRNA.
DR EMBL; M14216; AAA37609.1; -; mRNA.
DR EMBL; M17515; AAA37607.1; -; mRNA.
DR EMBL; M31312; AAA37610.1; -; Genomic_DNA.
DR EMBL; X04648; CAA28309.1; ALT_INIT; mRNA.
DR EMBL; U31801; AAA92707.1; -; mRNA.
DR EMBL; U31802; AAA92708.1; -; mRNA.
DR EMBL; U31803; AAA92709.1; -; mRNA.
DR EMBL; U31804; AAA92710.1; -; mRNA.
DR EMBL; M14276; AAA37605.1; -; mRNA.
DR EMBL; U51629; AAA97464.1; -; mRNA.
DR PIR; A40071; A40071.
DR PIR; B40071; FCMSG1.
DR PIR; I49660; I49660.
DR RefSeq; NP_034317.1; NM_010187.2.
DR AlphaFoldDB; P08101; -.
DR SMR; P08101; -.
DR BioGRID; 199619; 3.
DR ELM; P08101; -.
DR IntAct; P08101; 1.
DR MINT; P08101; -.
DR STRING; 10090.ENSMUSP00000027966; -.
DR MEROPS; I43.001; -.
DR GlyConnect; 342; 18 N-Linked glycans.
DR GlyGen; P08101; 5 sites, 32 N-linked glycans (1 site).
DR iPTMnet; P08101; -.
DR PhosphoSitePlus; P08101; -.
DR jPOST; P08101; -.
DR MaxQB; P08101; -.
DR PaxDb; P08101; -.
DR PRIDE; P08101; -.
DR ProteomicsDB; 272973; -. [P08101-1]
DR ProteomicsDB; 272974; -. [P08101-2]
DR ProteomicsDB; 272975; -. [P08101-3]
DR DNASU; 14130; -.
DR GeneID; 14130; -.
DR KEGG; mmu:14130; -.
DR UCSC; uc007dms.2; mouse. [P08101-1]
DR UCSC; uc007dmt.2; mouse. [P08101-2]
DR CTD; 2213; -.
DR MGI; MGI:95499; Fcgr2b.
DR eggNOG; ENOG502SVEW; Eukaryota.
DR InParanoid; P08101; -.
DR PhylomeDB; P08101; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2029481; FCGR activation.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14130; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fcgr2b; mouse.
DR PRO; PR:P08101; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P08101; protein.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0019864; F:IgG binding; IDA:MGI.
DR GO; GO:0019865; F:immunoglobulin binding; ISO:MGI.
DR GO; GO:0019772; F:low-affinity IgG receptor activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:MGI.
DR GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IMP:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:ARUK-UCL.
DR GO; GO:0006952; P:defense response; IMP:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:ARUK-UCL.
DR GO; GO:0032456; P:endocytic recycling; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0160006; P:Fc receptor-mediated immune complex endocytosis; IDA:UniProtKB.
DR GO; GO:0002434; P:immune complex clearance; ISO:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; IMP:MGI.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:MGI.
DR GO; GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
DR GO; GO:0050777; P:negative regulation of immune response; IMP:MGI.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IMP:MGI.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IMP:MGI.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:MGI.
DR GO; GO:0033030; P:negative regulation of neutrophil apoptotic process; ISO:MGI.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:MGI.
DR GO; GO:0001811; P:negative regulation of type I hypersensitivity; IMP:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0006911; P:phagocytosis, engulfment; IDA:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:ARUK-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:ARUK-UCL.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:ARUK-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR GO; GO:1905898; P:positive regulation of response to endoplasmic reticulum stress; IMP:ARUK-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; IMP:ARUK-UCL.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:ARUK-UCL.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW IgG-binding protein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT CHAIN 30..330
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT II"
FT /id="PRO_0000015143"
FT TOPO_DOM 30..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 50..106
FT /note="Ig-like C2-type 1"
FT DOMAIN 131..189
FT /note="Ig-like C2-type 2"
FT REGION 261..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 307..312
FT /note="ITIM motif"
FT COMPBIAS 272..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 290
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11035084"
FT MOD_RES 309
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250"
FT MOD_RES 326
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11035084"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 138..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 243..290
FT /note="ALPGNPDHREMGETLPEEVGEYRQPSGGSVPVSPGPPSGLEPTSSSPY ->
FT D (in isoform IIB2)"
FT /evidence="ECO:0000303|PubMed:3024012,
FT ECO:0000303|PubMed:8537115"
FT /id="VSP_002640"
FT VAR_SEQ 262..290
FT /note="GEYRQPSGGSVPVSPGPPSGLEPTSSSPY -> D (in isoform
FT IIB1')"
FT /evidence="ECO:0000303|PubMed:8683114"
FT /id="VSP_002641"
FT VARIANT 116
FT /note="S -> L (in strain: DBA/2; Ly17.2 allotype)"
FT /evidence="ECO:0000269|PubMed:2138587"
FT VARIANT 116
FT /note="S -> P (in strain: NZB; Ly17.1 allotype)"
FT /evidence="ECO:0000269|PubMed:2138587"
FT VARIANT 145
FT /note="L -> P"
FT VARIANT 161
FT /note="H -> L (in strain: DBA/2; Ly17.2 allotype)"
FT /evidence="ECO:0000269|PubMed:2138587"
FT VARIANT 161
FT /note="H -> Q (in strain: NZB; Ly17.1 allotype)"
FT /evidence="ECO:0000269|PubMed:2138587"
FT VARIANT 190
FT /note="L -> Q"
FT VARIANT 195
FT /note="P -> T (in strain: NZB)"
FT VARIANT 287
FT /note="S -> I (in strain: NZB)"
FT CONFLICT 270..278
FT /note="GSVPVSPGP -> LSACQPRA (in Ref. 1; AAA37608)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="A -> P (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36695 MW; A463B9EFF2717511 CRC64;
MESNWTVHVF SRTLCHMLLW TAVLNLAAGT HDLPKAVVKL EPPWIQVLKE DTVTLTCEGT
HNPGNSSTQW FHNGRSIRSQ VQASYTFKAT VNDSGEYRCQ MEQTRLSDPV DLGVISDWLL
LQTPQLVFLE GETITLRCHS WRNKLLNRIS FFHNEKSVRY HHYSSNFSIP KANHSHSGDY
YCKGSLGRTL HQSKPVTITV QGPKSSRSLP VLTIVAAVTG IAVAAIVIIL VSLVYLKKKQ
VPALPGNPDH REMGETLPEE VGEYRQPSGG SVPVSPGPPS GLEPTSSSPY NPPDLEEAAK
TEAENTITYS LLKHPEALDE ETEHDYQNHI
